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Open data
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Basic information
Entry | Database: PDB / ID: 5a9s | ||||||
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Title | NADPH complex of Imine Reductase from Amycolatopsis orientalis | ||||||
![]() | (IMINE REDUCTASE) x 2 | ||||||
![]() | OXIDOREDUCTASE / IMINE REDUCTASE / NADPH / AMINE | ||||||
Function / homology | ![]() 3-hydroxybutyrate dehydrogenase activity / methylated histone binding / NADP binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Man, H. / Aleku, G. / Turner, N.J. / Grogan, G. | ||||||
![]() | ![]() Title: Stereoselectivity and Structural Characterization of an Imine Reductase (IRED) from Amycolatopsis orientalis Authors: Aleku, G.A. / Man, H. / France, S.P. / Leipold, F. / Hussain, S. / Toca-Gonzalez, L. / Marchington, R. / Hart, S. / Turkenburg, J.P. / Grogan, G. / Turner, N.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 118.4 KB | Display | ![]() |
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PDB format | ![]() | 91.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 745.2 KB | Display | ![]() |
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Full document | ![]() | 751.4 KB | Display | |
Data in XML | ![]() | 13.8 KB | Display | |
Data in CIF | ![]() | 20.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3zgyS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: generate Matrix: (-0.9999, 0.009316, -0.009296), Vector: |
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Components
#1: Protein | Mass: 30490.572 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Protein | Mass: 30489.588 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
#3: Chemical | #4: Chemical | ChemComp-NAP / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.8 % / Description: NONE |
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Crystal grow | pH: 7.5 Details: 0.2 M CALCIUM ACETATE, 0.1 M TRIS PH 9.0, 8% (W/V) PEG 550 MME, 8% (W/V) PEG 20K WITH PROTEIN AT A CONCENTRATION OF 20 MG PER ML |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() ![]() ![]() ![]() ![]() |
Detector | Date: May 22, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97935 Å / Relative weight: 1 |
Reflection | Resolution: 2.06→49.29 Å / Num. obs: 32831 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 6.5 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 17.4 |
Reflection shell | Resolution: 2.06→2.11 Å / Redundancy: 6.4 % / Rmerge(I) obs: 0.7 / Mean I/σ(I) obs: 2.9 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3ZGY Resolution: 2.06→49.29 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.938 / SU B: 5.113 / SU ML: 0.135 / Cross valid method: THROUGHOUT / ESU R: 0.2 / ESU R Free: 0.175 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.985 Å2
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Refinement step | Cycle: LAST / Resolution: 2.06→49.29 Å
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